Nakoroxin antibacterial peptide
A small protein fragment that kills or slows the growth of bacteria; used only as a lab research tool.
A researcher, an agent, or an algorithm wrote down the sequence and picked a target to hit.
An AI model like OpenFold3 or AlphaFold built a 3D structure and scored how well it fits the binding site.
A second contributor repeated the computation on their own hardware and the scores matched.
A chemistry service or a researcher ordered the sequence, it was manufactured, and mass spectrometry confirmed the right molecule was produced.
A binding or activity measurement confirmed that it actually does what the computer predicted — or didn't.
Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.
If a molecule attacks tuberculosis, could it also fight the related lung bugs that kill cystic fibrosis patients?
Certain lung bacteria related to TB have become nearly impossible to treat, especially in cystic fibrosis patients. If this peptide targets the waxy outer shell these bacteria share with TB, it could open a door to treatments where almost none currently exist.
Does the peptide recognize and grip a unique sugar structure on TB's surface as its first step?
TB is coated in a complex sugar-fat shell that human cells do not have. If this peptide locks onto that structure first, it could explain why it kills TB while leaving human cells alone, and that targeting step could itself become a way to design better drugs.
Can a peptide kill bacteria without also damaging human cells, just because of the way it is shaped?
Many natural antibiotic peptides harm human red blood cells at roughly the same dose needed to kill bacteria, making them unsafe. If this peptide's rigid, clamp-like structure prevents it from punching through human cell membranes, it could have a much safer window for use in patients.
Could a peptide from venom kill the TB strains that have beaten every antibiotic we have?
Drug-resistant TB kills hundreds of thousands of people a year and options are running out. If this peptide attacks TB's unique waxy outer shell in a way no current drug does, resistant strains would have no ready defense against it.
Does having many internal bonds that lock a peptide's shape make it a better, more durable weapon against bacteria?
Most antibiotic peptides fall apart quickly in the bloodstream. If this peptide's eight internal locks give it a fortress-like shape that survives the body's digestive enzymes, it could stay active long enough to actually work as a medicine.
Instead of tearing bacteria apart, could this peptide simply stop them from building their own walls?
Many antibiotic peptides kill by ripping open bacterial membranes, which can also hurt human cells. If this peptide instead grabs onto a small molecule bacteria need to build their walls, blocking it like a wrench in gears, it could be both more precise and less likely to cause side effects.
Could scientists swap pieces of this peptide in and out, like building blocks, to tune it against specific resistant strains?
Discovering a new antibiotic scaffold from scratch takes years and large investments. If this peptide's frame stays stable while its surface loops can be swapped for pieces taken from other bacteria-killing molecules, researchers could mix and match to build a whole family of tailored drugs far faster.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.6902281641960144 | boltz-2 |
▸3-letter notation
▸recipeboltz-2 2.2.1
| parameter | value |
|---|---|
| model | boltz-2 2.2.1 |
| weights | — |
| hardware | vast_v100_32gb |
| mlx version | — |
| python | — |
| random seed | 1 |
| msa strategy | none_monomer |
| runtime | — |
| predicted by | — |
| predicted at | 2026-05-23 |
▸citationbibtex
@peptide{pep05521,
sequence = {ECYRKSDIVTCEPWQKFCYREVTFFPNHPVYLSGCASECTETNSKWCCTTDKCNRARGG},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {computed}
}